A hallmark of neurodegenerative diseases caused by polyglutamine expansion is the
abnormal accumulation of mutant proteins into ubiquitin-positive inclusions. The local build …

Lysine residues are one of the main sites for posttranslational modifications of proteins, and
lysine ubiquitination of the Machado-Joseph disease protein ataxin-3 is implicated in its …

Intranuclear inclusion bodies (IBs) are the histopathologic markers of multiple protein folding
diseases. IB formation has been extensively studied using fluorescent fusion products of …

Expansions of preexisting polyglutamine (polyQ) tracts in at least nine different proteins
cause devastating neurodegenerative diseases. There are many unique features to these …

The polyglutamine (polyQ) diseases, such as Huntington's disease and several types of
spinocerebellar ataxias, are a group of inherited neurodegenerative diseases that are …

The presence and aggregation of misfolded proteins has deleterious effects in the nervous
system. Among the various diseases caused by misfolded proteins is the family of the …

Alterations in the ubiquitin-proteasome system (UPS) have been reported in several
neurodegenerative disorders characterized by protein misfolding and aggregation, including …

Trinucleotide repeat (TNR) expansions are present in a wide range of genes involved in
several neurological disorders, being directly involved in the molecular mechanisms …

Polyglutamine diseases, such as Huntington's disease, are among the most common
inherited neurodegenerative disorders. They share salient clinical and pathological features …

Background Aggregation and cytotoxicity of mutant proteins containing an expanded
number of polyglutamine (polyQ) repeats is a hallmark of several diseases, including …